Cathepsin B,L Inhibitor | CTSB, inhibitor

Cathepsin B,L Inhibitor (Z-FF-FMK)

Cat. Num. AAA655413

• Purity: Molecular Biology Grade; 95% by HPLC analysis
• Synonyms: Cathepsin B; L Inhibitor; L Inhibitor (Z-FF-FMK); CTSB; inhibitor

• Purity/Purification: Molecular Biology Grade; 95% by HPLC analysis
• Sequence: Z-Phe-Phe-FMK (FMK, fluoromethyl ketone)

• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -20 degree C. Aliquots are stable for 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Related Product Information for CTSB, inhibitor

Cathepsins are localized primarily in lysosomes or endosomes, but translocated to the cytosol during apoptosis. The translocation allows these proteases to interact with caspases or other apoptosis signaling mechanisms. Studies show that cathepsins cleave certain caspases, and caspase inhibitors can inhibit cathepsin activity in vitro.

Product Categories/Family for CTSB, inhibitor

Molecular Biology; MB-Cathepsin

NCBI and Uniprot Product Information

• NCBI GI #: 27806671
• NCBI GeneID: 281105
• NCBI Accession #: NP_776456.1
• NCBI GenBank Nucleotide #: NM_174031.2
• UniProt Accession #: P07688; Q3ZC03
• Molecular Weight: 462D
• NCBI Official Full Name: cathepsin B
• NCBI Official Synonym Full Names: cathepsin B
• NCBI Official Symbol: CTSB
• NCBI Protein Information: cathepsin B; BCSB
• UniProt Protein Name: Cathepsin B
• Protein Family: Cathepsin
• UniProt Gene Name: CTSB
• UniProt Entry Name: CATB_BOVIN

Uniprot Description

Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

Catalytic activity: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.

Subunit structure: Interacts with SRPX2

By similarity. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.

Subcellular location: Lysosome. Melanosome

By similarity. Secreted › extracellular space

By similarity.

Sequence similarities: Belongs to the peptidase C1 family.